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LSG1_DROME
ID   LSG1_DROME              Reviewed;         606 AA.
AC   Q9W590;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Large subunit GTPase 1 homolog;
DE            EC=3.6.1.-;
DE   AltName: Full=Nucleostemin-3;
GN   Name=Ns3; Synonyms=l(1)G0431; ORFNames=CG14788;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=18628395; DOI=10.1101/gad.1670508;
RA   Kaplan D.D., Zimmermann G., Suyama K., Meyer T., Scott M.P.;
RT   "A nucleostemin family GTPase, NS3, acts in serotonergic neurons to
RT   regulate insulin signaling and control body size.";
RL   Genes Dev. 22:1877-1893(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-279, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: GTPase required for the nuclear export of the 60S ribosomal
CC       subunit. Probably acts by mediating the release of Nmd3 from the 60S
CC       ribosomal subunit after export into the cytoplasm. Regulator of body
CC       size; acts in serotonergic neurons to regulate insulin signaling and
CC       thus exerts global growth control. {ECO:0000269|PubMed:18628395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18628395}.
CC       Note=Punctate distribution.
CC   -!- TISSUE SPECIFICITY: Expressed in larval serotonergic neurons.
CC       {ECO:0000269|PubMed:18628395}.
CC   -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC       characterized by a circular permutation of the GTPase motifs described
CC       by a G4-G1-G3 pattern.
CC   -!- DISRUPTION PHENOTYPE: Larvae reach less than 60% of normal size and
CC       have fewer and smaller cells, the adults that survive exhibit normal
CC       body proportions and are healthy. In the brains excess serotonin and
CC       insulin accumulate, while peripheral insulin pathway activation is low.
CC       {ECO:0000269|PubMed:18628395}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. LSG1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; AE014298; AAF45628.1; -; Genomic_DNA.
DR   EMBL; AL035632; CAB38462.1; -; Genomic_DNA.
DR   EMBL; AY047556; AAK77288.1; -; mRNA.
DR   RefSeq; NP_001284779.1; NM_001297850.1.
DR   RefSeq; NP_569915.1; NM_130559.3.
DR   AlphaFoldDB; Q9W590; -.
DR   SMR; Q9W590; -.
DR   BioGRID; 57654; 10.
DR   IntAct; Q9W590; 2.
DR   STRING; 7227.FBpp0070284; -.
DR   iPTMnet; Q9W590; -.
DR   PaxDb; Q9W590; -.
DR   PRIDE; Q9W590; -.
DR   DNASU; 31097; -.
DR   EnsemblMetazoa; FBtr0070297; FBpp0070284; FBgn0266284.
DR   EnsemblMetazoa; FBtr0339578; FBpp0308653; FBgn0266284.
DR   GeneID; 31097; -.
DR   KEGG; dme:Dmel_CG14788; -.
DR   CTD; 31097; -.
DR   FlyBase; FBgn0266284; Ns3.
DR   VEuPathDB; VectorBase:FBgn0266284; -.
DR   eggNOG; KOG1424; Eukaryota.
DR   HOGENOM; CLU_011072_2_0_1; -.
DR   InParanoid; Q9W590; -.
DR   OMA; VNKADMM; -.
DR   OrthoDB; 839833at2759; -.
DR   PhylomeDB; Q9W590; -.
DR   SignaLink; Q9W590; -.
DR   BioGRID-ORCS; 31097; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31097; -.
DR   PRO; PR:Q9W590; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0266284; Expressed in oviduct (Drosophila) and 37 other tissues.
DR   ExpressionAtlas; Q9W590; baseline and differential.
DR   Genevisible; Q9W590; DM.
DR   GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR   GO; GO:0051168; P:nuclear export; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:FlyBase.
DR   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR043358; GNL1-like.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45709; PTHR45709; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Growth regulation; GTP-binding;
KW   Hydrolase; Nucleotide-binding; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..606
FT                   /note="Large subunit GTPase 1 homolog"
FT                   /id="PRO_0000324559"
FT   DOMAIN          165..395
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         213..216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         344..351
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         388..391
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         276
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
SQ   SEQUENCE   606 AA;  70246 MW;  147566CF5CDFB9EB CRC64;
     MGKKNKGGAP NLGRQLIKDR FGHTQRRKVD NDTMLHTTEL QDGYDWGRLN LSSVTEESSF
     QAFLRTAELA GTEFQAEKLN ITFVNPKQRV GLLSKTQEQR MHQKHDEHRD QLKIPRRPKW
     TKETSAEELV RAENEAFLDW RRDLALLQED EEILMTPYEK NLEFWRQLWR VVERSDVVVQ
     IVDARNPLLF RSADLERYVK EVEPSKMNMI LVNKSDLLTE EQRRHWAEYF DSEGIRTAFY
     SATLVEEELK REAEECLDSF PEVQQLRRAV EEIKQSLDSV EDALNVIEQK YKTIPETQND
     ELPRLPGDKN SPRLLSRLEL IEFLRNIYTG PRHTEQHVTV GMVGYPNVGK SSTINSLMTV
     KKVSVSATPG KTKRFQTLFL DKDILLCDCP GLVMPSFVLT KADMLLNGIL PIDQMRDHVP
     AVNLLCERIP RHVLEDKYGI VIAKPLEGED MERPPHSEEL LLAYGYNRGF MTSNGQPDQA
     RSARYVLKDY VNGRLLYAMS PPSVPQTEYH TFPERQRRVI EESQLPGQQQ RAMRINKSTS
     KELDNQFFSD KPTHAHVKGR TNFPNVRLAN DGSLVAGNDP AAKPWRHVKK ERREKLRKKF
     SHLDEH
 
 
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